The goal of the MacCHESS Research Resource is to support macromolecular crystallography at the Cornell High Energy Synchrotron Source (CHESS). This will be accomplished by developing and providing specialized instrumentation for crystallographic studies by our national user community and by performing core research that advances the frontiers of synchrotron radiation research. We will continue to provide service to the macromolecular crystallography community with special emphasis on monochromatic oscillation data collection and MAD phasing techniques. The facilities at CHESS should be particularly useful for small crystals, crystals with large unit cells, weakly diffracting crystals and crystals susceptible to radiation damage. Central to our goal is the development of more user friendly hardware, software and operational procedures that will make trips to CHESS more productive. MacCHESS will support macromolecular crystallography on beamlines A-1 (monochromatic oscillation data), B-2 (Laue diffraction), F-1 (monochromatic oscillation data with biohazard containment facilities) and F-2 (MAD phasing). Access to these experimental stations will be based on the CHESS peer- reviewed proposal system. Future core research will include establishment of a centralized data reduction facility, implementation of CCD-based X-ray detectors, construction of apparatus for MAD phasing on station F-2, development of microfocusing optics for X-ray diffraction studies of microcrystals, upgrade of station A-1 to take advantage of the new A line wiggler, implementation of low-temperature techniques, investigation of high energy X-ray diffraction, general optics development and undulator experimentation. In addition, we will continue to develop software for data collection and analysis and to make the software more user friendly. MacCHESS will provide trained staff to assist users in setting up beamlines, designing experiments and processing X-ray diffraction data. CCD-detector development will be supplemented by acquisition of additional image plate scanners and additional electronic and computing equipment will be purchased to refurbish a synchrotron radiation laboratory that has been productive for more than ten years. All of these developments will bring nearer the goal of rapid visualization of macromolecular structure. Finally we will continue to provide training and dissemination through maintenance of operation manuals, preparation of a MacChess brochure, on-site instruction, organization of workshops, presentations at meetings, presentation of invited seminars and production of training videos for CHESS facilities and low temperature techniques.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001646-13
Application #
2281563
Study Section
Special Emphasis Panel (ZRG7-SSS-Z (01))
Project Start
1983-09-01
Project End
1998-08-31
Budget Start
1995-09-01
Budget End
1996-08-31
Support Year
13
Fiscal Year
1995
Total Cost
Indirect Cost
Name
Cornell University
Department
Biochemistry
Type
Schools of Arts and Sciences
DUNS #
City
Ithaca
State
NY
Country
United States
Zip Code
14850
Kozlov, Guennadi; Wong, Kathy; Gehring, Kalle (2018) Crystal structure of the Legionella effector Lem22. Proteins 86:263-267
Ménade, Marie; Kozlov, Guennadi; Trempe, Jean-François et al. (2018) Structures of ubiquitin-like (Ubl) and Hsp90-like domains of sacsin provide insight into pathological mutations. J Biol Chem 293:12832-12842
Xu, Jie; Kozlov, Guennadi; McPherson, Peter S et al. (2018) A PH-like domain of the Rab12 guanine nucleotide exchange factor DENND3 binds actin and is required for autophagy. J Biol Chem 293:4566-4574
Dean, Dexter N; Rana, Pratip; Campbell, Ryan P et al. (2018) Propagation of an A? Dodecamer Strain Involves a Three-Step Mechanism and a Key Intermediate. Biophys J 114:539-549
Chen, Yu Seby; Kozlov, Guennadi; Fakih, Rayan et al. (2018) The cyclic nucleotide-binding homology domain of the integral membrane protein CNNM mediates dimerization and is required for Mg2+ efflux activity. J Biol Chem 293:19998-20007
Xu, Caishuang; Kozlov, Guennadi; Wong, Kathy et al. (2016) Crystal Structure of the Salmonella Typhimurium Effector GtgE. PLoS One 11:e0166643
Cogliati, Massimo; Zani, Alberto; Rickerts, Volker et al. (2016) Multilocus sequence typing analysis reveals that Cryptococcus neoformans var. neoformans is a recombinant population. Fungal Genet Biol 87:22-9
Oot, Rebecca A; Kane, Patricia M; Berry, Edward A et al. (2016) Crystal structure of yeast V1-ATPase in the autoinhibited state. EMBO J 35:1694-706
Lucido, Michael J; Orlando, Benjamin J; Vecchio, Alex J et al. (2016) Crystal Structure of Aspirin-Acetylated Human Cyclooxygenase-2: Insight into the Formation of Products with Reversed Stereochemistry. Biochemistry 55:1226-38
Bauman, Joseph D; Harrison, Jerry Joe E K; Arnold, Eddy (2016) Rapid experimental SAD phasing and hot-spot identification with halogenated fragments. IUCrJ 3:51-60

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